The mould Aspergillus ochraceus produces and liberates into the culture medium a proteolytic
enzyme. It was highly purified and obtained in crystalline form by ethanol-calcium
precipitation. The enzyme (molecular weight approximately 20,000) hydrolyses typical
trypsin and chymotrypsin substrates as well as proteins, such as casein, haemoglobin
and fibrin. It is inhibited by blood plasma antiproteinases. In animal experiments,
the enzyme shows relatively low toxicity as well as antithrombotic and thrombolytic
effects, even at doses lower than the plasma antiproteinase level. Experimentally
produced clotting and deposition thrombi in peripheral veins and arteries as well
as in coronary arteries are removed by proteolytic degradation. Based on first clinical
studies, the enzyme, Awegillase(R), is considered a suitable tool for both local and
systemic thrombolytic therapy.